4kdq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
+
{{STRUCTURE_4kdq| PDB=4kdq | SCENE= }}
 +
===Crystal structure of the hemagglutinin of A/Xinjiang/1/2006 virus===
 +
{{ABSTRACT_PUBMED_23794001}}
-
The entry 4kdq is ON HOLD until Paper Publication
+
==Function==
 +
[[http://www.uniprot.org/uniprot/C5HMM2_9INFA C5HMM2_9INFA]] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore (By similarity).[RuleBase:RU003324][SAAS:SAAS008980_004_327643] [[http://www.uniprot.org/uniprot/Q6J0Q2_9INFA Q6J0Q2_9INFA]] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore (By similarity).[RuleBase:RU003324][SAAS:SAAS008980_004_327643]
-
Authors: Lu, X., Shi, Y., Zhang, W., Zhang, Y., Qi, J., Gao, G.F.
+
==About this Structure==
 +
[[4kdq]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/xinjiang/1/2006(h5n1)) Influenza a virus (a/xinjiang/1/2006(h5n1))], [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/chicken/guangdong/174/04(h5n1)) Influenza a virus (a/chicken/guangdong/174/04(h5n1))] and [http://en.wikipedia.org/wiki/Unidentified_influenza_virus Unidentified influenza virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KDQ OCA].
-
Description: Crystal structure of the hemagglutinin of A/Xinjiang/1/2006 virus
+
==Reference==
 +
<ref group="xtra">PMID:023794001</ref><references group="xtra"/><references/>
 +
[[Category: Unidentified influenza virus]]
 +
[[Category: Gao, G F.]]
 +
[[Category: Lu, X.]]
 +
[[Category: Qi, J.]]
 +
[[Category: Shi, Y.]]
 +
[[Category: Zhang, W.]]
 +
[[Category: Zhang, Y.]]
 +
[[Category: Homotrimer]]
 +
[[Category: Viral protein]]
 +
[[Category: Virus attachment and membrane fusion]]

Revision as of 12:54, 24 July 2013

Template:STRUCTURE 4kdq

Contents

Crystal structure of the hemagglutinin of A/Xinjiang/1/2006 virus

Template:ABSTRACT PUBMED 23794001

Function

[C5HMM2_9INFA] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore (By similarity).[RuleBase:RU003324][SAAS:SAAS008980_004_327643] [Q6J0Q2_9INFA] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore (By similarity).[RuleBase:RU003324][SAAS:SAAS008980_004_327643]

About this Structure

4kdq is a 6 chain structure with sequence from Influenza a virus (a/xinjiang/1/2006(h5n1)), Influenza a virus (a/chicken/guangdong/174/04(h5n1)) and Unidentified influenza virus. Full crystallographic information is available from OCA.

Reference

  • Lu X, Shi Y, Zhang W, Zhang Y, Qi J, Gao GF. Structure and receptor-binding properties of an airborne transmissible avian influenza A virus hemagglutinin H5 (VN1203mut). Protein Cell. 2013 Jun 20. PMID:23794001 doi:10.1007/s13238-013-3906-z

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools